Assembly and specific recognition of k29- and k33-linked polyubiquitin

Protein ubiquitination regulates many cellular processes via attachment of structurally and functionally distinct ubiquitin (Ub) chains. Several atypical chain types have remained poorly characterized because the enzymes mediating their assembly and receptors with specific binding properties have be...

Celý popis

Uložené v:
Podrobná bibliografia
Vydané v:Molecular cell Ročník 58; číslo 1; s. 95 - 109
Hlavní autori: Michel, Martin A, Elliott, Paul R, Swatek, Kirby N, Simicek, Michal, Pruneda, Jonathan N, Wagstaff, Jane L, Freund, Stefan M V, Komander, David
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: United States 02.04.2015
Predmet:
Amino Acid Sequence
Crystallography, X-Ray
Endopeptidases - chemistry
Endopeptidases - genetics
Endopeptidases - metabolism
Escherichia coli - genetics
Escherichia coli - metabolism
HEK293 Cells
Humans
Hydrophobic and Hydrophilic Interactions
Lysine - chemistry
Lysine - metabolism
Models, Molecular
Molecular Sequence Data
Proteasome Endopeptidase Complex - metabolism
Protein Binding
Protein Conformation
Protein Processing, Post-Translational
Protein Structure, Tertiary
Proteolysis
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Signal Transduction
Ubiquitin - chemistry
Ubiquitin - genetics
Ubiquitin - metabolism
Ubiquitin-Protein Ligases - chemistry
Ubiquitin-Protein Ligases - genetics
Ubiquitin-Protein Ligases - metabolism
Ubiquitination
ISSN:1097-4164
On-line prístup:Zistit podrobnosti o prístupe
Tagy: Pridať tag
Žiadne tagy, Buďte prvý, kto otaguje tento záznam!
Popis
Shrnutí:Protein ubiquitination regulates many cellular processes via attachment of structurally and functionally distinct ubiquitin (Ub) chains. Several atypical chain types have remained poorly characterized because the enzymes mediating their assembly and receptors with specific binding properties have been elusive. We found that the human HECT E3 ligases UBE3C and AREL1 assemble K48/K29- and K11/K33-linked Ub chains, respectively, and can be used in combination with DUBs to generate K29- and K33-linked chains for biochemical and structural analyses. Solution studies indicate that both chains adopt open and dynamic conformations. We further show that the N-terminal Npl4-like zinc finger (NZF1) domain of the K29/K33-specific deubiquitinase TRABID specifically binds K29/K33-linked diUb, and a crystal structure of this complex explains TRABID specificity and suggests a model for chain binding by TRABID. Our work uncovers linkage-specific components in the Ub system for atypical K29- and K33-linked Ub chains, providing tools to further understand these unstudied posttranslational modifications.
Bibliografia:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1097-4164
DOI:10.1016/j.molcel.2015.01.042